Isolation and Characterization of Collagenase from Bacillus Subtilis (Ehrenberg, 1835); ATCC 6633 for Degrading Fish Skin Collagen Waste from Cirata Reservoir, Indonesia

Objective: This study aims to isolate and characterize the collagen isolated from the skin of patin fish.Method: Collagen isolation consisted of three steps, namely deproteinization process using NaOH solution concentration of 0,05 M and long soaking time for 3x24 hours; immersion in CH3COOH solution with a concentration of 0,05 M and long soaking time 3x24 hours; Furthermore, collagen was extracted with water at 40°C for 2 hours. The isolated collagen was tested for characteristics including chemical and physical properties compared to commercial collagen.Results: Chemical characteristics of collagen isolated from patin fish skin isolation compared to commercial collagen, respectively: 6,55% and 6,68% water content; ash content of 0,19% and 0,18%; protein content 93,63% and 97,42% and fat content 0,41% and 0,30%; The metal content in the collagen isolated from the skin of patin fish and commercial collagen is below the threshold (Pb); 0,5 mg/kg. Amino acid test results from patin fish skin collagen obtained glycine (234381,88 mg/kg), proline (109404,17 mg/kg), alanine (83988,79 mg/kg), arginine (80918,44 mg/kg) and glutamate (87315,88 mg/kg). The physical characteristics of the patin fish skin collagen showed the presence of amide group A (3286,7cm-1), amide B (2947,23cm-1), amide I (1651,07cm-1), amide II (1450,47cm-1), and amide III (1246,02 cm-1).Conclusion: Patin fish skin can be isolated into collagen that meets the quality requirements of collagen as a cosmetic preparation.

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Partial Characterization of Fish Skin Collagen Cross-Linked by N-Hydroxysuccinimide Activated Adipic Acid

Journal of Aquatic Food Product Technology ◽

10.1080/10498850.2012.693578 ◽

2013 ◽

Vol 23 (1) ◽

pp. 44-58 ◽

Cited By ~ 7

Author(s):

Min Zhang ◽

Guoying Li

Keyword(s):

Adipic Acid ◽

Partial Characterization ◽

Fish Skin ◽

Skin Collagen ◽

Fish Skin Collagen

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Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes

Nutrients ◽

10.3390/nu13082657 ◽

2021 ◽

Vol 13 (8) ◽

pp. 2657

Author(s):

Maryam Atef ◽

Yasmina Ait Chait ◽

Seyed Mahdi Ojagh ◽

Ali Mohammad Latifi ◽

Mina Esmaeili ◽

...

Keyword(s):

Antibacterial Activity ◽

Degree Of Hydrolysis ◽

Fish Skin ◽

Small Peptides ◽

Skin Collagen ◽

Dependent Inhibition ◽

Acetone Fractionation ◽

Chain Lengths ◽

Peptide Fractions ◽

Fish Skin Collagen

This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight < 10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.

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